ID A0A0G1LLB4_9BACT Unreviewed; 291 AA.
AC A0A0G1LLB4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:KKT96565.1};
GN ORFNames=UW97_C0008G0022 {ECO:0000313|EMBL:KKT96565.1};
OS Parcubacteria group bacterium GW2011_GWA2_45_15.
OC Bacteria.
OX NCBI_TaxID=1618833 {ECO:0000313|EMBL:KKT96565.1, ECO:0000313|Proteomes:UP000034700};
RN [1] {ECO:0000313|EMBL:KKT96565.1, ECO:0000313|Proteomes:UP000034700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKT96565.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCKK01000008; KKT96565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1LLB4; -.
DR Proteomes; UP000034700; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd14852; LD-carboxypeptidase; 1.
DR Gene3D; 3.30.1380.10; -; 1.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR003709; Pept_M15B.
DR PANTHER; PTHR34385; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR34385:SF1; PEPTIDOGLYCAN L-ALANYL-D-GLUTAMATE ENDOPEPTIDASE CWLK; 1.
DR Pfam; PF02557; VanY; 1.
DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:KKT96565.1};
KW Hydrolase {ECO:0000313|EMBL:KKT96565.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KKT96565.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 137..260
FT /note="Peptidase M15B"
FT /evidence="ECO:0000259|Pfam:PF02557"
SQ SEQUENCE 291 AA; 33583 MW; 52B134FD2796F6A1 CRC64;
MKTFSRYKLY LQPALLISVI VALFLAGYVA FEYRLLGDEL RISEEENLEI SAQLEEVRKD
RFDLSELSKY QQFIIDSFTG QISSIGNTVG TLEKLAQTDK ELLKKYSKVY FLNENYVPAK
LTQVEKIYTF DGGENFLIHA EVWPYLKRLL DAASASDIEL LVVSAFRSFD TQASLKSEYR
VTYGAGTANQ FSADQGYSEH QLGTSVDFTT AAVGAMFSKF KSDPAYQWLI NNAHRYGFVL
SYPEGNTYYK FEPWHWRFVG VSLAEMLNKE NKYFYDLDQR EIDAYLIKLF E
//